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At least 19 recordsLinked to original sources
PubMed1981

Evidence for a species of nuclear actin distinct from cytoplasmic and muscles actins.

Nuclear actin (protein BJ) has been isolated from the chromatin of Novikoff hepatoma ascites cells and purified to homogeneity by selective extraction, Sepharose CL-6B chromatography, and preparative polyacrylamide gel electrophoresis. A comparison of nuclear and cytoplasmic actins from Novikoff hepatoma cells and rabbit muscle actin was made by amino acid analysis, isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and two-dimensional peptide mapping procedures. By these criteria, all of the proteins compared are actins, but each is chemically distinct. It was concluded, therefore, that nuclear actin is similar to, but not identical with, cytoplasmic actin isolated from Novikoff hepatoma cells. A striking similarity in peptide charge and migration as shown by peptide map analysis was observed for nuclear and rabbit skeletal muscle actins. This may indicate that nuclear actin has the capacity for contractile function. In addition, the actins synthesized in Novikoff hepatoma cells may results from more than two structural genes.

Actins↗
PubMed1984

Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes.

Nuclei of amphibian oocytes contain large amounts of actin, mostly in unpolymerized or short-polymer form. When antibodies to actin or actin-binding proteins (fragmin and the actin modulator from mammalian smooth muscle) are injected into nuclei of living oocytes of Pleurodeles waltlii, transcription of the lampbrush chromosomes, but not of the rRNA genes, is inhibited. When transcription is repressed by drugs or RNA is digested by microinjection of RNAase into oocyte nuclei, an extensive meshwork of actin filament bundles is seen in association with the isolated lampbrush chromosomes. These observations indicate a close relationship between the state of nuclear actin and transcriptional activity and suggest that nuclear actin may be involved in transcriptional events concerning protein-coding genes.

Actins↗
PubMed1980

Dissolution of cytoplasmic actin bundles and the induction of nuclear actin bundles by dimethyl sulfoxide.

Within 30 minutes of exposure to medium containing 10% dimethyl sulfoxide, PtK2 cells begin to round up and lose their cytoplasmic actin bundles. At the same time, bundles of actin filaments appear in the nuclei of the cells. One to 2 hours after the dimethyl sulfoxide is removed from the medium, the cells revert to their flattened shape, losing the nuclear actin bundles and regaining the cytoplasmic bundles.

Actins↗
PubMed2004

Nuclear actin and myosin I are required for RNA polymerase I transcription.

The presence of actin and nuclear myosin I (NMI) in the nucleus suggests a role for these motor proteins in nuclear functions. We have investigated the role of actin and nuclear myosin I (NMI) in the transcription of ribosomal RNA genes (rDNA). Both proteins are associated with rDNA and are required for RNA polymerase I (Pol I) transcription. Microinjection of antibodies against actin or NMI, as well as short interfering RNA-mediated depletion of NMI, decreased Pol I transcription in vivo, whereas overexpression of NMI augmented pre-rRNA synthesis. In vitro, recombinant NMI activated Pol I transcription, and antibodies to NMI or actin inhibited Pol I transcription both on naked DNA and pre-assembled chromatin templates. Whereas actin associated with Pol I, NMI bound to Pol I through the transcription-initiation factor TIF-IA. The association with Pol I requires phosphorylation of TIF-IA at Ser 649 by RSK kinase, indicating a role for NMI in the growth-dependent regulation of rRNA synthesis.

Actins↗
PubMed2004

Unpolymerized nuclear actin is involved in the activation of CSF-1 gene transcription.

Nuclear actin is a nuclear component in many kinds of eukaryotic cells but its function is still not clear. In this study, we overexpressed actin in nuclei and found that it promoted transcription of the CSF-1 gene, both exogenous and endogenous, approximately two-fold. Cytochalasin B did not affect this function of nuclear actin. Our results suggest that nuclear actin plays a role in regulating CSF-1 gene transcription, and this role does not depend on actin polymerization.

Actins↗
PubMed1984

Decondensation of human spermatozoal chromatin by nuclear actin polymerization.

A critical relationship exists between nuclear actin polymerization and decondensation of sperm chromatin. Characteristic decondensation phenomena were brought about by the protein S-1 of heavy meromyosin of rabbit skeletal muscle in sperm that had undergone the acrosome reaction. Sperm treated with only calcium or only ionophore were not affected by the S-1 trigger, and the nucleus remained in the condensed state. Since S-1 specifically binds to actin, it was possible to demonstrate this phenomenon at the ultrastructural level. Maybe there are switches that operate at different steps for events leading to syngamy and fertilization. No switch can be operative until the preceding event has prepared the sperm for entering the next phase. The operations are performed in a perfect sequential order. This investigation leads to the conclusion that decondensation of sperm chromatin is brought about by nuclear actin polymerization.

Acrosome↗
PubMed2003

Nuclear actin and protein 4.1: essential interactions during nuclear assembly in vitro.

Structural protein 4.1, which has crucial interactions within the spectrin-actin lattice of the human red cell membrane skeleton, also is widely distributed at diverse intracellular sites in nucleated cells. We previously showed that 4.1 is essential for assembly of functional nuclei in vitro and that the capacity of 4.1 to bind actin is required. Here we report that 4.1 and actin colocalize in mammalian cell nuclei using fluorescence microscopy and, by higher-resolution detergent-extracted cell whole-mount electron microscopy, are associated on nuclear filaments. We also devised a cell-free assay using Xenopus egg extract containing fluorescent actin to follow actin during nuclear assembly. By directly imaging actin under nonperturbing conditions, the total nuclear actin population is retained and visualized in situ relative to intact chromatin. We detected actin initially when chromatin and nuclear pores began assembling. As nuclear lamina assembled, but preceding DNA synthesis, actin distributed in a reticulated pattern throughout the nucleus. Protein 4.1 epitopes also were detected when actin began to accumulate in nuclei, producing a diffuse coincident pattern. As nuclei matured, actin was detected both coincident with and also independent of 4.1 epitopes. To test whether acquisition of nuclear actin is required for nuclear assembly, the actin inhibitor latrunculin A was added to Xenopus egg extracts during nuclear assembly. Latrunculin A strongly perturbed nuclear assembly and produced distorted nuclear structures containing neither actin nor protein 4.1. Our results suggest that actin as well as 4.1 is necessary for nuclear assembly and that 4.1-actin interactions may be critical.

Actins↗
PubMed2000

Searching for a function for nuclear actin.

The abundant cytoskeletal protein actin has numerous cytoplasmic roles. Although there are many reports of the presence of actin in the nucleus, in general they have been discounted as artifactual. However, recent work has begun to provide evidence for important roles for actin in nuclear processes ranging from chromatin remodelling to splicing. In addition, several regulators of actin polymerization are localized to the nucleus or translocate to the nucleus in a regulated manner, suggesting that there is some function of actin in the nucleus that is subject to regulation. This review discusses the evidence for actin in the nucleus and summarizes recent work suggesting that actin or actin-related proteins are involved in the regulation of nuclear processes such as chromatin remodelling.

Actins↗
PubMed1989

Identification of a widespread nuclear actin binding protein.

The many different cellular functions so far shown to involve actin and to be regulated by specific actin binding proteins are located primarily, if not exclusively, in the cytoplasm. Actin is also found in the nucleus of various cells, but because of the problems of cell fractionation the significance of nuclear actin has remained unclear. The large amphibian oocyte nucleus (germinal vesicle), however, can be isolated manually with little cytoplasmic contamination. This nucleus contains high concentrations (4-6 mg ml-1) of mostly soluble, although polymerization-competent beta- and gamma-actin, which exists in a nucleocytoplasmic exchange pool. The findings that drastic effects on transcription and chromosome morphology are caused by the injection of actin antibodies or actin binding proteins into germinal vesicles, and that a factor required for accurate transcription by RNA polymerase II is actin, suggest that nuclear actin is involved in specific nuclear functions. We have recently identified two main components in Xenopus laevis oocytes with actin binding activities; one of these activities is Ca2+-dependent, is located predominantly, if not exclusively, in the cytoplasm and is attributable to gelsolin. Here we report that the second component, having a Ca2+-independent activity, is a heterodimeric acting binding protein; this protein is markedly enriched in the nuclei of oocytes and somatic cells of amphibia, but also occurs in nuclei of other vertebrate cells.

Actins↗
PubMed2006

Dynamic nuclear actin assembly by Arp2/3 complex and a baculovirus WASP-like protein.

Diverse bacterial and viral pathogens induce actin polymerization in the cytoplasm of host cells to facilitate infection. Here, we describe a pathogenic mechanism for promoting dynamic actin assembly in the nucleus to enable viral replication. The baculovirus Autographa californica multiple nucleopolyhedrovirus induced nuclear actin polymerization by translocating the host actin-nucleating Arp2/3 complex into the nucleus, where it was activated by p78/83, a viral Wiskott-Aldrich syndrome protein (WASP)-like protein. Nuclear actin assembly by p78/83 and Arp2/3 complex was essential for viral progeny production. Recompartmentalizing dynamic host actin may represent a conserved mode of pathogenesis and reflect viral manipulation of normal functions of nuclear actin.

Actin-Related Protein 2-3 Complex↗
PubMed1997

Quantitative changes in cytoskeletal and nuclear actins during cellular transformation.

Actin, a highly conserved protein comprising cell stress fibers and other cellular structures, is found in both the cytoplasm and nucleus of cells and responds to both epigenetic signals and altered gene expression occurring during tumorigenesis. We have previously shown that changes in the cytoplasmic F- and G-actin ratios reflect bladder cancer risk. To determine whether nuclear actin is also altered and how nuclear and cytoplasmic actin alterations are interrelated in transformation, an in vitro model of carcinogen-induced transformation consisting of 2 human uroepithelial cell lines immortalized by infection with SV-40 was studied. One line, HUC-PC, is tumorigenic in nude mice after incubation with the carcinogen 4-ABP, the other, HUC-BC, is not. Cytoplasmic and nuclear F- and G-actin were determined by QFIA on individual cells using fluorochrome-labeled phallicidin and DNase, I, respectively. Before exposure to 4-ABP, the PC cells had lower cytoplasmic F-actin content, higher cytoplasmic G-actin content, but similar levels of nuclear G- and F-actin in comparison to the BC cells. After incubation with 4-ABP, F-actin decreased and G-actin increased in both cytoplasm and nuclei of PC cells and cytoplasmic F-actin fibers were lost, but only cytoplasmic actin was altered in the BC cells. Northern blot analysis showed the expression of the beta-actin gene was only approximately 20% lower in 4-ABP-treated PC cells than in untreated controls, indicating the cellular change in actin was attributed to a shift between F- and G-actin proteins rather than to net actin synthesis.

Actins↗
PubMed2005

Nuclear actin is partially associated with Cajal bodies in human cells in culture and relocates to the nuclear periphery after infection of cells by adenovirus 5.

Cajal bodies are intra-nuclear structures enriched in proteins involved in transcription and mRNA processing. In this study, immunofluorescence microscopy experiments using a highly specific antibody to actin revealed nuclear actin spots that colocalized in part with p80 coilin-positive Cajal bodies. Actin remained associated with Cajal bodies in cells extracted to reveal the nuclear matrix. Adenovirus infection, which is known to disassemble Cajal bodies, resulted in loss of actin from these structures late in infection. In infected cells, nuclear actin was observed to relocate to structures at the periphery of the nucleus, inside the nuclear envelope. Based on these findings, it is suggested that actin may play an important role in the organization or function of the Cajal body.

Actins↗
PubMed1979

Nuclear actin and histones from the myxomycete Physarum flavicomum.

A method was established for the isolation and purification of nuclei in high yield from the microplasmodia of Physarum flavicomum. Purified nuclei was resistant to breakage by methods commonly employed for isolated plant and animal nuclei. Incubation of nuclei with 5 mM dithiothreitol at pH 9.2 was found to be the simplest and most effective method for breaking the nuclei. Several methods for the extraction of nuclear protein were compared. Incubation of nuclear lysates with either 2 M NaCl, with or without 5 M urea, or 1 M CaCl2 resulted in the extraction of nuclear actin together with histones. The histones were chemically fractionated into the five basic groups common to other eucaryotic tissue. Amino acid analyses of the total histone were also performed. Nuclear actin was found to have a molecular weight of 41,000 +/- 4,000 daltons as determined by SDS polyacrylamide gel electrophoresis. The amino acid composition of the nuclear actin was established.

Actins↗
PubMed1980

Dynamics of nuclear actin bundle induction by dimethyl sulfoxide and factors affecting its development.

We have reported in a previous paper that dimethyl sulfoxide (DMSO) induces the formation of huge bundles of actin filaments in the nuclei of Dictyostelium mucoroides. The present study was performed to provide electron microscope data on the induction of nuclear actin bundles, illustrating both their formation and their reversion, as well as on the effects of various factors on the induction. The large nuclear bundles of actin appeared after 20--30 min of treatment with 10% DMSO. A DMSO concentration of 5 or 10% was optimal for the induction of the bundles. The nuclear actin bundle reverted to the original morphology within 5 min after removing DMSO. Induction of nuclear actin bundles was inhibited by Mg++ and low temperatures, but not by Na+, K+, Ca++, ATP, 3'5'-cyclic adenosine monophosphate (cAMP), phosphate buffer, or cytochalasin B. Neither NaN3 nor cycloheximide totally inhibited the induction of the bundles.

Actins↗
PubMed2006

Nuclear actin: to polymerize or not to polymerize.

The form and function of actin in the nucleus have been enigmatic for over 30 years. Recently actin has been assigned numerous functional roles in the nucleus, but its form remains a mystery. The intricate relationship between actin form and function in the cytoplasm implies that understanding the structural properties of nuclear actin is elementary to fully understanding its function. In this issue, McDonald et al. (p. 541) use fluorescence recovery after photobleaching (FRAP) to tackle the question of whether nuclear actin exists as monomers or polymers.

Actins↗
PubMed2001

Nuclear actin and actin-related proteins in chromatin remodeling.

The existence and function of actin in the nucleus has been hotly debated for forty years. Recently, beta-actin was found to be a component of mammalian SWI/SNF-like BAF chromatin remodeling complexes and still more recently other SWI/SNF-related chromatin remodeling complexes in yeast, flies, and man. Although the function of actin in these chromatin remodeling complexes is only starting to be explored, the fact that actin is one of the most regulated proteins in the cell suggests that control of nuclear actin may be a critical regulatory point in the control of chromatin remodeling. Actin rapidly shuttles between the nucleus and the cytoplasm offering additional sites and modes of regulation. In addition, actin-related proteins (Arps) are also components of these chromatin remodeling complexes and have been implicated in transcriptional control in yeast. The observation that the BAF chromatin remodeling complex in which actin was originally identified, is also a human tumor suppressor complex necessary for the actions of the retinoblastoma protein indicates that the study of nuclear actin is likely to contribute to understanding cell growth control.

Actins↗
PubMed1987

Nuclear actin and transport of RNA.

The role of nuclear actin filaments in the RNA transport was investigated. Mouse lymphoma cells, L5178Y, were labeled for 20 min with 3H-uridine, and the isolated nuclei were incubated in a medium consisting of 0.25 M sucrose, 10 mM Tris-HCl (pH 7.5), 2 mM CaCl2, 1 mM ATP and 1mM PMSF. Release of the rapidly labeled RNA from the nuclei was temperature-dependent and was stimulated by ATP. Phalloidin, an inhibitor of actin filament depolymerization, had no effect on the system at 10 or 100 micrograms/ml. Therefore, actin filament depolymerization may not be involved in the transport of RNA.

Actins↗